Component

Copper(II) bis(L-histidinate) / Cu(His)2

Context-specific entity; species, compartment and exposure are stated on each claim.

1 recorded relationships. Experimental role, claim status and evidence remain attached to each record.

How nutrients influence it

Every nutrient with a recorded effect on this component, credited to the nutrient that acted rather than the chapter that recorded it. Open a nutrient to see the findings and the conditions they were measured under.

How nutrients reach it in more than one step

Chains of two or more recorded steps that end here, grouped by the nutrient they start from. Each step is a separate finding, so a chain is a route a mechanism could take, not proof that it does.

Tracing routes…

What it does

Every recorded relationship this component is part of, grouped by its role. Plain wording comes first; the technical statement follows.

Recorded relationships

What acts on it

  1. Purified human LAT1 transported Cu(His)2 without the internal counter-substrate required for ordinary amino-acid antiport.

    Experimental context and source evidence
    evidence_access
    Primary full text
    experimental_model
    Reconstituted human LAT1; radiotracer uptake, copper mass spectrometry and mutagenesis; representative assay 40 micromolar histidine plus 20 micromolar copper sulfate.
    limitations
    This in-vitro uniport finding does not establish human copper delivery, safety or treatment efficacy.
    nutrient_topic
    L-Histidine collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · L-Histidine
    plain_language
    Binding copper changed how the histidine-containing species crossed this transporter.
    primary_references
    LAT1 (SLC7A5) catalyzes copper(histidinate) transport switching from antiport to uniport mechanism. · 2023 · https://pubmed.ncbi.nlm.nih.gov/37692288/ · DOI 10.1016/j.isci.2023.107738
    transport_effect
    raises Transported without the internal counter-substrate ordinary antiport needs, so this record is a uniport measurement.
    transport_pool
    the proteoliposome interior Transported without the internal counter-substrate ordinary antiport needs, so this record is a uniport measurement.

    L-Histidine: supply, catabolism, histamine, receptors and cross-nutrient mechanisms (2026-09-19) · lines 82–88

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Reconstituted human LAT1; radiotracer uptake, copper mass spectrometry and mutagenesis; representative assay 40 micromolar histidine plus 20 micromolar copper sulfate. · source_derived_draft · unverified_draft

    ## histidine-lat1-copper-complex Binding copper changed how the histidine-containing species crossed this transporter. Purified human LAT1 transported Cu(His)2 without the internal counter-substrate required for ordinary amino-acid antiport. Model: Reconstituted human LAT1; radiotracer uptake, copper mass spectrometry and mutagenesis; representative assay 40 micromolar histidine plus 20 micromolar copper sulfate. Limitations: This in-vitro uniport finding does not establish human copper delivery, safety or treatment efficacy. Evidence access: Primary full text LAT1 (SLC7A5) catalyzes copper(histidinate) transport switching from antiport to uniport mechanism. · 2023 · https://pubmed.ncbi.nlm.nih.gov/37692288/ · DOI 10.1016/j.isci.2023.107738
    Complete structured claim and evidence

In the sources

Preserved passages that mention this component, quoted exactly. Open one to read it in context.

    This is a research prototype built from draft material. It is not medical advice, and its statements still await verification against the original studies.

    Evidence, AI assistance and curation standards